New drug shows promise in treating osteoporosis, calcium-related disorders

WEST LAFAYETTE, Ind. — Osteoporosis is a particularly nasty ailment that results in one’s bones becoming weak, brittle, and easily broken. Now, researchers from Purdue University have created a new form of a pre-existing drug already being used to treat osteoporosis. They say this newer version may represent a fresh treatment option with less side-effects for people dealing with calcium-related disorders.

All humans require the hormone called calcitonin in order to maintain normal calcium stability. Osteoporosis patients usually don’t have enough calcitonin, so they’re prescribed calcitonin as a treatment. When taken regularly, this drug blocks bone resorption, ultimately leading to increased bone mass.

This new form of human calcitonin is more stable than earlier varieties of the peptide drug. It was invented when the team at Purdue created a prodrug form of the peptide hormone. These changes should increase the drug’s effectiveness against osteoporosis and related problems considerably.

‘Our approach will increase therapeutic potential of human calcitonin’

All of that sounds great, but human calcitonin ends up undergoing fibrillation when placed in a water solution. This leads to reduced therapeutic efficiency. To overcome the problem, many osteoporosis patients have been prescribed salmon calcitonin instead. Salmon calcitonin does not fibrillate as much as human calcitonin, but it also isn’t nearly as helpful and offers more harmful side-effects.

“The technology can help make these calcitonin drugs safer and more effective,” says professor of physical and industrial pharmacy Elizabeth Topp in a university release. “Our approach will increase the therapeutic potential of human calcitonin, promising a more effective option to replace salmon calcitonin for osteoporosis and related disorders.”

To decrease the potential for fibrillation and increase the therapeutic benefits of human calcitonin, researchers added a phosphate group to specific amino acid residues.

“Many promising new peptide drugs tend to form fibrils,” Topp concludes. “This technology provides a way to stabilize them in a reversible way so that the stabilizing modification comes off when the drug is given to the patient.”

The study is published in Biophysical Journal.

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